[Purification and study of influenza virus neuraminidases]

Purified preparations of polypeptides of neuraminidases of 10 influenza A virus strains were obtained by two-dimensional electrophoresis of proteins in polyacrylamide gel in which proteins with intact disulphid bonds were used for phoresis in the first direction and those with destroyed disulphid bonds for phoresis in the second direction. Fractionation of tryptic tyrosinil-peptides of neuraminidases labeled in vitro with radioactive iodine was carried out by two-dimensional dispersal by means of electrophoresis and chromatography. Comparison of oligopeptide maps of neuraminidases gave both expected results (for some specimens, correlation of similarities in peptide maps with similar antigenic structure) and some unexpected findings.